BVDV P7蛋白的原核表达及其生物信息学分析
发布时间：2018-10-16 19:39
【摘要】：为了对BVDV-1 P7蛋白进行原核表达及生物信息学分析,采用RT-PCR的方法扩增BVDV NADL株BVDV-1 P7的ORF,扩增产物经Bam H I、Sal I双酶切后插入原核表达载体p EGX4T-1(+),构建P7基因原核表达载体并将其转化至工程菌E.coli BL21(DE3)中进行诱导表达,并对其进行生物信息学预测。结果表明,成功扩增并构建了BVDV NADL株的BVDV-1 P7原核表达载体,命名p EGX4T-1-P7。SDS-PAGE和Western blot表明,在分子质量34 k Da的位置出现与预期大小一致的蛋白条带;生物信息学结果表明在P7蛋白有信号肽,存在疏水区。该研究成功的表达了P7蛋白,该蛋白是一个疏水性蛋白,为其进一步的功能研究奠定了坚实的基础。
[Abstract]:For prokaryotic expression and bioinformatics analysis of BVDV-1 P7 protein, The ORF, amplification product of BVDV-1 P7 of BVDV NADL strain was amplified by RT-PCR and inserted into prokaryotic expression vector p EGX4T-1 (), after being digested with Bam H Il-Sal I and then transformed into E.coli BL21 (DE3) to induce expression. The bioinformatics prediction was carried out. The results showed that the prokaryotic expression vector of BVDV-1 P7 of BVDV NADL strain was successfully amplified and constructed. The identification of p EGX4T-1-P7.SDS-PAGE and Western blot showed that the protein bands were consistent with the expected size at the position of 34 k Da. Bioinformatics results showed that P7 protein had signal peptide and hydrophobic region. This study successfully expressed P7 protein, a hydrophobic protein, which laid a solid foundation for further functional study.
【作者单位】： 黑龙江八一农垦大学动物科技学院;
【基金】：黑龙江省青年科学基金(QC2015031) 兽医生物技术国家重点实验室开放课题基金(SKLVBF201508)
【分类号】：S852.65
[Abstract]:For prokaryotic expression and bioinformatics analysis of BVDV-1 P7 protein, The ORF, amplification product of BVDV-1 P7 of BVDV NADL strain was amplified by RT-PCR and inserted into prokaryotic expression vector p EGX4T-1 (), after being digested with Bam H Il-Sal I and then transformed into E.coli BL21 (DE3) to induce expression. The bioinformatics prediction was carried out. The results showed that the prokaryotic expression vector of BVDV-1 P7 of BVDV NADL strain was successfully amplified and constructed. The identification of p EGX4T-1-P7.SDS-PAGE and Western blot showed that the protein bands were consistent with the expected size at the position of 34 k Da. Bioinformatics results showed that P7 protein had signal peptide and hydrophobic region. This study successfully expressed P7 protein, a hydrophobic protein, which laid a solid foundation for further functional study.
【作者单位】： 黑龙江八一农垦大学动物科技学院;
【基金】：黑龙江省青年科学基金(QC2015031) 兽医生物技术国家重点实验室开放课题基金(SKLVBF201508)
【分类号】：S852.65
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本文编号：2275428
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